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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kumar, Nitin Radhakrishnan, Abhijith Bolla, Jani Reddy Purdy, Georgiana E. Chou, Tsung-han Tringides, Marios L. Rajashankar, Kanagalaghatta R. Su, Chih-chia Yu, Edward W. Wright, Catherine C. Lei, Hsiang-ting |
| Description | Author Affiliation: Radhakrishnan A ( From the Department of Chemistry and.); Kumar N ( From the Department of Chemistry and.); Wright CC ( the Department of Molecular Microbiology and Immunology, Oregon Health and Sciences University, Portland, Oregon 97239, and.); Chou TH ( the Department of Physics and Astronomy, Iowa State University, Ames, Iowa 50011.); Tringides ML ( From the Department of Chemistry and.); Bolla JR ( From the Department of Chemistry and.); Lei HT ( From the Department of Chemistry and.); Rajashankar KR ( the Northeastern Collaborative Access Team and Department of Chemistry and Chemical Biology, Cornell University, Argonne National Laboratory, Argonne, Illinois 60439.); Su CC ( the Department of Physics and Astronomy, Iowa State University, Ames, Iowa 50011.); Purdy GE ( the Department of Molecular Microbiology and Immunology, Oregon Health and Sciences University, Portland, Oregon 97239, and.); Yu EW ( From the Department of Chemistry and the Department of Physics and Astronomy, Iowa State University, Ames, Iowa 50011, ewyu@iastate.edu.) |
| Abstract | Recent work demonstrates that the MmpL (mycobacterial membrane protein large) transporters are dedicated to the export of mycobacterial lipids for cell wall biosynthesis. An MmpL transporter frequently works with an accessory protein, belonging to the MmpS (mycobacterial membrane protein small) family, to transport these key virulence factors. One such efflux system in Mycobacterium tuberculosis is the MmpS5-MmpL5 transporter. The expression of MmpS5-MmpL5 is controlled by the MarR-like transcriptional regulator Rv0678, whose open reading frame is located downstream of the mmpS5-mmpL5 operon. To elucidate the structural basis of Rv0678 regulation, we have determined the crystal structure of this regulator, to 1.64 Å resolution, revealing a dimeric two-domain molecule with an architecture similar to members of the MarR family of transcriptional regulators. Rv0678 is distinct from other MarR regulators in that its DNA-binding and dimerization domains are clustered together. These two domains seemingly cooperate to bind an inducing ligand that we identified as 2-stearoylglycerol, which is a fatty acid glycerol ester. The structure also suggests that the conformational change leading to substrate-mediated derepression is primarily caused by a rigid body rotational motion of the entire DNA-binding domain of the regulator toward the dimerization domain. This movement results in a conformational state that is incompatible with DNA binding. We demonstrate using electrophoretic mobility shift assays that Rv0678 binds to the mmpS5-mmpL5, mmpS4-mmpL4, and the mmpS2-mmpL2 promoters. Binding by Rv0678 was reversed upon the addition of the ligand. These findings provide new insight into the mechanisms of gene regulation in the MarR family of regulators. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 23 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-06-06 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Mycobacterium Tuberculosis Metabolism Amino Acid Sequence Crystallography, X-Ray DNA Primers Dimerization Molecular Sequence Data Chemistry Polymerase Chain Reaction Sequence Homology, Amino Acid Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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